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Titolo:
Solution structure of grb2 reveals extensive flexibility necessary for target recognition
Autore:
Yuzawa, S; Yokochi, M; Hatanaka, H; Ogura, K; Kataoka, M; Miura, K; Mandiyan, V; Schlessinger, J; Inagaki, F;
Indirizzi:
Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biol Struct, Sapporo, Hokkaido 0600812, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600812 oro, Hokkaido 0600812, Japan Gakushuin Univ, Inst Biomol Sci, Tokyo 1718588, Japan Gakushuin Univ Tokyo Japan 1718588 Inst Biomol Sci, Tokyo 1718588, Japan Tokyo Metropolitan Inst Med Sci, Dept Mol Physiol, Tokyo 113, Japan Tokyo Metropolitan Inst Med Sci Tokyo Japan 113 hysiol, Tokyo 113, Japan Nara Inst Sci & Technol, Dept Mat Sci, Nara 6300101, Japan Nara Inst Sci &Technol Nara Japan 6300101 Mat Sci, Nara 6300101, Japan NYU Med Ctr, New York, NY 10016 USA NYU Med Ctr New York NY USA 10016NYU Med Ctr, New York, NY 10016 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 3, volume: 306, anno: 2001,
pagine: 527 - 537
SICI:
0022-2836(20010223)306:3<527:SSOGRE>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAGNETIC-RESONANCE RELAXATION; RECEPTOR TYROSINE KINASES; SMALL-ANGLE-SCATTERING; N-15 NMR RELAXATION; TERMINAL SH3 DOMAIN; MODEL-FREE APPROACH; X-RAY-SCATTERING; CONSOLIDATED LIGANDS; SIGNALING PATHWAY; BACKBONE DYNAMICS;
Keywords:
NMR; SAXS; Grb2; flexibility; solution structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Inagaki, F Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biol Struct, Sapporo, Hokkaido 0600812, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600812 do 0600812, Japan
Citazione:
S. Yuzawa et al., "Solution structure of grb2 reveals extensive flexibility necessary for target recognition", J MOL BIOL, 306(3), 2001, pp. 527-537

Abstract

Grb2 is an adaptor protein composed of a single SH2 domain flanked by two SH3 domains. Grb2 functions as an important evolutionary conserved link between a variety of cell membrane receptors and the Ras/MAP kinase-signaling cascade. Here, we describe the solution structure of Grb2 as revealed by NMR and small angle X-ray scattering measurements. We demonstrate that Grb2 is a flexible protein in which the C-terminal SH3 domain is connected to theSH2 domain via a flexible linker. This is in contrast to the previously described Grb2 crystal structure, which showed a compact structure with intramolecular contact between two SH3 domains. Binding experiments on Grb2 and peptides containing two different proline-rich sequences indicate that Grb2adapts the relative position and orientation of the two SH3 domains to bind bivalently to the target peptide sequences. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 07:33:37